Caspase-3


NameCaspase-3
Synonyms3.4.22.56 Apopain CASP-3 CPP-32 CPP32 Cysteine protease CPP32 Protein Yama SCA-1 SREBP cleavage activity 1
Gene NameCASP3
OrganismHuman
Amino acid sequence
>lcl|BSEQ0016333|Caspase-3
MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTG
MTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLS
HGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDD
DMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVN
RKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH
Number of residues277
Molecular Weight31607.58
Theoretical pI6.51
GO Classification
Functions
    cysteine-type endopeptidase activity involved in execution phase of apoptosis
    aspartic-type endopeptidase activity
    cysteine-type endopeptidase activity involved in apoptotic process
    cysteine-type endopeptidase activity
    peptidase activity
    phospholipase A2 activator activity
    cyclin-dependent protein serine/threonine kinase inhibitor activity
Processes
    hippocampus development
    learning or memory
    sensory perception of sound
    regulation of cysteine-type endopeptidase activity involved in apoptotic process
    neuron apoptotic process
    negative regulation of activated T cell proliferation
    programmed cell death
    keratinocyte differentiation
    apoptotic process
    response to amino acid
    response to X-ray
    heart development
    T cell homeostasis
    apoptotic signaling pathway
    cellular response to organic cyclic compound
    negative regulation of apoptotic process
    platelet formation
    activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c
    erythrocyte differentiation
    cell fate commitment
    neurotrophin TRK receptor signaling pathway
    neuron differentiation
    glial cell apoptotic process
    hippo signaling
    positive regulation of neuron apoptotic process
    response to hypoxia
    negative regulation of B cell proliferation
    intrinsic apoptotic signaling pathway
    negative regulation of cyclin-dependent protein serine/threonine kinase activity
    extrinsic apoptotic signaling pathway
    cellular response to DNA damage stimulus
    wound healing
    execution phase of apoptosis
    proteolysis
    response to nicotine
    cellular component disassembly involved in execution phase of apoptosis
    extracellular matrix disassembly
    response to glucose
    B cell homeostasis
    extracellular matrix organization
    response to glucocorticoid
    apoptotic DNA fragmentation
    response to drug
    response to cobalt ion
    extrinsic apoptotic signaling pathway in absence of ligand
    response to estradiol
    response to lipopolysaccharide
    response to antibiotic
    response to UV
    response to hydrogen peroxide
    response to tumor necrosis factor
Components
    plasma membrane
    cytosol
    nucleoplasm
    death-inducing signaling complex
    membrane raft
    nucleus
General FunctionPhospholipase a2 activator activity
Specific FunctionInvolved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage.
Transmembrane Regions
GenBank Protein ID561666
UniProtKB IDP42574
UniProtKB Entry NameCASP3_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0016334|Caspase-3 (CASP3)
ATGGAGAACACTGAAAACTCAGTGGATTCAAAATCCATTAAAAATTTGGAACCAAAGATC
ATACATGGAAGCGAATCAATGGACTCTGGAATATCCCTGGACAACAGTTATAAAATGGAT
TATCCTGAGATGGGTTTATGTATAATAATTAATAATAAGAATTTTCATAAAAGCACTGGA
ATGACATCTCGGTCTGGTACAGATGTCGATGCAGCAAACCTCAGGGAAACATTCAGAAAC
TTGAAATATGAAGTCAGGAATAAAAATGATCTTACACGTGAAGAAATTGTGGAATTGATG
CGTGATGTTTCTAAAGAAGATCACAGCAAAAGGAGCAGTTTTGTTTGTGTGCTTCTGAGC
CATGGTGAAGAAGGAATAATTTTTGGAACAAATGGACCTGTTGACCTGAAAAAAATAACA
AACTTTTTCAGAGGGGATCGTTGTAGAAGTCTAACTGGAAAACCCAAACTTTTCATTATT
CAGGCCTGCCGTGGTACAGAACTGGACTGTGGCATTGAGACAGACAGTGGTGTTGATGAT
GACATGGCGTGTCATAAAATACCAGTGGAGGCCGACTTCTTGTATGCATACTCCACAGCA
CCTGGTTATTATTCTTGGCGAAATTCAAAGGATGGCTCCTGGTTCATCCAGTCGCTTTGT
GCCATGCTGAAACAGTATGCCGACAAGCTTGAATTTATGCACATTCTTACCCGGGTTAAC
CGAAAGGTGGCAACAGAATTTGAGTCCTTTTCCTTTGACGCTACTTTTCATGCAAAGAAA
CAGATTCCATGTATTGTTTCCATGCTCACAAAAGAACTCTATTTTTATCACTAA
GenBank Gene IDU13737
GeneCard IDNone
GenAtlas IDCASP3
HGNC IDHGNC:1504
Chromosome Location4
Locus4q34
References
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  2. Tewari M, Quan LT, O'Rourke K, Desnoyers S, Zeng Z, Beidler DR, Poirier GG, Salvesen GS, Dixit VM: Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell. 1995 Jun 2;81(5):801-9.[7774019 ]
  3. Pelletier M, Cartron PF, Delaval F, Meflah K, Vallette FM, Oliver L: Caspase 3 activation is controlled by a sequence located in the N-terminus of its large subunit. Biochem Biophys Res Commun. 2004 Mar 26;316(1):93-9.[15003516 ]
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  7. Goldberg YP, Nicholson DW, Rasper DM, Kalchman MA, Koide HB, Graham RK, Bromm M, Kazemi-Esfarjani P, Thornberry NA, Vaillancourt JP, Hayden MR: Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract. Nat Genet. 1996 Aug;13(4):442-9.[8696339 ]
  8. Mannick JB, Hausladen A, Liu L, Hess DT, Zeng M, Miao QX, Kane LS, Gow AJ, Stamler JS: Fas-induced caspase denitrosylation. Science. 1999 Apr 23;284(5414):651-4.[10213689 ]
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  10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309.[19413330 ]
  11. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17.[21269460 ]
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  13. Bienvenut WV, Sumpton D, Martinez A, Lilla S, Espagne C, Meinnel T, Giglione C: Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-alpha-acetylation features. Mol Cell Proteomics. 2012 Jun;11(6):M111.015131. doi: 10.1074/mcp.M111.015131. Epub 2012 Jan 5.[22223895 ]
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